Isolation and purification of native amylase / cellulase enzyme of Bacillus amyloliquefaciens UMAS 1002

Wan Adnawani, Meor Osman (2008) Isolation and purification of native amylase / cellulase enzyme of Bacillus amyloliquefaciens UMAS 1002. [Final Year Project Report] (Unpublished)

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Abstract

Bacillus amyloliquefaciens UMAS 1002 strain was screened and isolated by Apun et. al (2000). It produced amylolytic and cellulolytic enzymes in extracellular medium when it as grown in media consist of sago pith waste. In this project amylase and cellulase was not completely purified from the culture supernatant. Purification of these enzymes involved two steps that comprised ammonium sulphate precipitation and hydrophobic interaction chromatography. Hydrophobic interaction chromatography method managed to purify the protein up to 80% purity. The enzyme activity was determined using dinitrosalicylic acid (DNS) enzyme assay and protein content was detennined using Bradford protein assay. The specific activity of amylase and celulLase after HIC method is 0.0655 umol/min/mg and 0.0110 umol/min/mg. SDS-PAGE was used to delermine the purity and molecular weight of amylase and cellulase enzymes. The molecular weight of the enzymes that has been purified was around 50-75 kDa.

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